prolinhidroxiláz

prolyl hydroxylase, also known as prolinhidroxiláz in some languages, is an enzyme that plays a crucial role in the post-translational modification of proteins, particularly collagen. This enzyme catalyzes the hydroxylation of proline residues to form hydroxyproline, which is essential for the stability and proper functioning of collagen molecules.

The hydroxylation process requires molecular oxygen, ferrous iron, alpha-ketoglutarate, and ascorbate as cofactors. Without this modification, collagen would be unable to form its characteristic triple helix structure, leading to weakened connective tissue.

Prolyl hydroxylase is found in most eukaryotic organisms and is highly conserved across species. In humans, deficiencies in this enzyme or its cofactors can lead to various connective tissue disorders. The enzyme also functions as an oxygen sensor in mammalian cells, regulating hypoxia-inducible factor (HIF) stability under low oxygen conditions.

The discovery of prolyl hydroxylase's role in oxygen sensing has opened new avenues for therapeutic interventions in conditions such as anemia, ischemic diseases, and cancer. Research continues to explore the enzyme's potential as a drug target for various medical conditions.